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Volumn 12, Issue 5, 2013, Pages 1294-1305

Quantitative Liquid Chromatography-Mass Spectrometry-Multiple Reaction Monitoring (LC-MS-MRM) analysis of site-specific glycoforms of haptoglobin in liver disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA(2 3,6,8)NEURAMINIDASE; BETA(1 4)GALACTOSIDASE; ENZYME; EXOGLYCOSIDASE; FUCOSE; GLYCOPEPTIDE; HAPTOGLOBIN; UNCLASSIFIED DRUG;

EID: 84877619420     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.023325     Document Type: Article
Times cited : (83)

References (48)
  • 1
    • 0034789412 scopus 로고    scopus 로고
    • The bittersweet promise of glycobiology
    • Dove, A. (2001) The bittersweet promise of glycobiology. Nat. Biotechnol. 19, 913-917
    • (2001) Nat. Biotechnol. , vol.19 , pp. 913-917
    • Dove, A.1
  • 2
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • DOI 10.1126/science.291.5512.2364
    • Helenius, A., and Aebi, M. (2001) Intracellular functions of N-linked glycans. Science 291, 2364-2369 (Pubitemid 32231791)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 3
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., Gnad, F., Wiśniewski, J. R., and Mann, M. (2010) Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897-907
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4
  • 4
    • 79961035468 scopus 로고    scopus 로고
    • Genome-wide evolutionary conservation of N-glycosylation sites
    • Park, C., and Zhang, J. (2011) Genome-wide evolutionary conservation of N-glycosylation sites. Mol. Biol. Evol. 28, 2351-2357
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2351-2357
    • Park, C.1    Zhang, J.2
  • 5
    • 3543071604 scopus 로고    scopus 로고
    • Sialidase and malignancy: A minireview
    • DOI 10.1023/B:GLYC.0000024250.48506.bf
    • Miyagi, T., Wada, T., Yamaguchi, K., and Hata, K. (2004) Sialidase and malignancy: A minireview. Glycoconj. J. 20, 189-198 (Pubitemid 39024047)
    • (2003) Glycoconjugate Journal , vol.20 , Issue.3 , pp. 189-198
    • Miyagi, T.1    Wada, T.2    Yamaguchi, K.3    Hata, K.4
  • 6
    • 44449153943 scopus 로고    scopus 로고
    • Functional roles of N-glycans in cell signaling and cell adhesion in cancer
    • DOI 10.1111/j.1349-7006.2008.00839.x
    • Zhao, Y. Y., Takahashi, M., Gu, J. G., Miyoshi, E., Matsumoto, A., Kitazume, S., and Taniguchi, N. (2008) Functional roles of N-glycans in cell signaling and cell adhesion in cancer. Cancer Sci. 99, 1304-1310 (Pubitemid 351761717)
    • (2008) Cancer Science , vol.99 , Issue.7 , pp. 1304-1310
    • Zhao, Y.-Y.1    Takahashi, M.2    Gu, J.-G.3    Miyoshi, E.4    Matsumoto, A.5    Kitazume, S.6    Taniguchi, N.7
  • 8
    • 34548402664 scopus 로고    scopus 로고
    • Quantitative glycomics of human whole serum glycoproteins based on the standardized protocol for liberating N-glycans
    • DOI 10.1074/mcp.T600063-MCP200
    • Kita, Y., Miura, Y., Furukawa, J., Nakano, M., Shinohara, Y., Ohno, M., Takimoto, A., and Nishimura, S. (2007) Quantitative glycomics of human whole serum glycoproteins based on the standardized protocol for liberating N-glycans. Mol. Cell. Proteomics 6, 1437-1445 (Pubitemid 47365441)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.8 , pp. 1437-1445
    • Kita, Y.1    Miura, Y.2    Furukawa, J.-I.3    Nakano, M.4    Shinohara, Y.5    Ohno, M.6    Takimoto, A.7    Nishimura, S.-I.8
  • 11
    • 77955155580 scopus 로고    scopus 로고
    • High Throughput quantification of N-glycans using one-pot sialic acid modification and matrix assisted laser desorption ionization time-of-flight mass spectrometry
    • Gil, G. C., Iliff, B., Cerny, R., Velander, W. H., and Van Cott, K. E. (2010) High Throughput quantification of N-glycans using one-pot sialic acid modification and matrix assisted laser desorption ionization time-of-flight mass spectrometry. Anal. Chem. 82, 6613-6620
    • (2010) Anal. Chem. , vol.82 , pp. 6613-6620
    • Gil, G.C.1    Iliff, B.2    Cerny, R.3    Velander, W.H.4    Van Cott, K.E.5
  • 13
    • 84862168794 scopus 로고    scopus 로고
    • Structural analysis of N- and O-glycans released from glycoproteins
    • Jensen, P. H., Karlsson, N. G., Kolarich, D., and Packer, N. H. (2012) Structural analysis of N- and O-glycans released from glycoproteins. Nat. Protoc. 7, 1299-1310
    • (2012) Nat. Protoc. , vol.7 , pp. 1299-1310
    • Jensen, P.H.1    Karlsson, N.G.2    Kolarich, D.3    Packer, N.H.4
  • 14
    • 0030571019 scopus 로고    scopus 로고
    • A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles
    • DOI 10.1006/abio.1996.0351
    • Guile, G. R., Rudd, P. M., Wing, D. R., Prime, S. B., and Dwek, R. A. (1996) A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles. Anal. Biochem. 240, 210-226 (Pubitemid 26304265)
    • (1996) Analytical Biochemistry , vol.240 , Issue.2 , pp. 210-226
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Prime, S.B.4    Dwek, R.A.5
  • 15
    • 50649102341 scopus 로고    scopus 로고
    • N-Glycan profiling in the study of human aging
    • Vanhooren, V., Laroy, W., Libert, C., and Chen, C. (2008) N-Glycan profiling in the study of human aging. Biogerontology 9, 351-356
    • (2008) Biogerontology , vol.9 , pp. 351-356
    • Vanhooren, V.1    Laroy, W.2    Libert, C.3    Chen, C.4
  • 16
    • 28044433453 scopus 로고    scopus 로고
    • Solid-phase permethylation of glycans for mass spectrometric analysis
    • DOI 10.1002/rcm.2210
    • Kang, P., Mechref, Y., Klouckova, I., and Novotny, M. V. (2005) Solid-phase permethylation of glycans for mass spectrometric analysis. Rapid Commun. Mass Spectrom. 19, 3421-3428 (Pubitemid 41691916)
    • (2005) Rapid Communications in Mass Spectrometry , vol.19 , Issue.23 , pp. 3421-3428
    • Kang, P.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4
  • 19
    • 84862238705 scopus 로고    scopus 로고
    • Determination of site-specific glycan heterogeneity on glycoproteins
    • Kolarich, D., Jensen, P. H., Altmann, F., and Packer, N. H. (2012) Determination of site-specific glycan heterogeneity on glycoproteins. Nat. Protoc. 7, 1285-1298
    • (2012) Nat. Protoc. , vol.7 , pp. 1285-1298
    • Kolarich, D.1    Jensen, P.H.2    Altmann, F.3    Packer, N.H.4
  • 21
    • 82455188350 scopus 로고    scopus 로고
    • Application of nano-LC-based glycomics toward biomarker discovery
    • Hua, S., Lebrilla, C., and An, H. J. (2011) Application of nano-LC-based glycomics toward biomarker discovery. Bioanalysis 3, 2573-2585
    • (2011) Bioanalysis , vol.3 , pp. 2573-2585
    • Hua, S.1    Lebrilla, C.2    An, H.J.3
  • 22
    • 77956261162 scopus 로고    scopus 로고
    • High-throughput profiling of the serum N-glycome on capillary electrophoresis microfluidics systems: Toward clinical implementation of GlycoHepatoTest
    • Vanderschaeghe, D., Szekrényes, A., Wenz, C., Gassmann, M., Naik, N., Bynum, M., Yin, H., Delanghe, J., Guttman, A., and Callewaert, N. (2010) High-throughput profiling of the serum N-glycome on capillary electrophoresis microfluidics systems: toward clinical implementation of GlycoHepatoTest. Anal. Chem. 82, 7408-7415
    • (2010) Anal. Chem. , vol.82 , pp. 7408-7415
    • Vanderschaeghe, D.1    Szekrényes, A.2    Wenz, C.3    Gassmann, M.4    Naik, N.5    Bynum, M.6    Yin, H.7    Delanghe, J.8    Guttman, A.9    Callewaert, N.10
  • 24
  • 25
    • 34548012656 scopus 로고    scopus 로고
    • Comparative glycomic mapping through quantitative permethylation and stable-isotope labeling
    • DOI 10.1021/ac062098r
    • Kang, P., Mechref, Y., Kyselova, Z., Goetz, J. A., and Novotny, M. V. (2007) Comparative glycomic mapping through quantitative permethylation and stable-isotope labeling. Anal. Chem. 79, 6064-6073 (Pubitemid 47282315)
    • (2007) Analytical Chemistry , vol.79 , Issue.16 , pp. 6064-6073
    • Kang, P.1    Mechref, Y.2    Kyselova, Z.3    Goetz, J.A.4    Novotny, M.V.5
  • 27
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • DOI 10.1038/nbt827
    • Zhang, H., Li, X. J., Martin, D. B., and Aebersold, R. (2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling, and mass spectrometry. Nat. Biotechnol. 21, 660-666 (Pubitemid 36638093)
    • (2003) Nature Biotechnology , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.-J.2    Martin, D.B.3    Aebersold, R.4
  • 28
    • 80052327326 scopus 로고    scopus 로고
    • Stable isotope-labeled hydrophobic hydrazide reagents for the relative quantification of N-linked glycans by electrospray ionization mass spectrometry
    • Walker, S. H., Budhathoki-Uprety, J., Novak, B. M., and Muddiman, D. C. (2011) Stable isotope-labeled hydrophobic hydrazide reagents for the relative quantification of N-linked glycans by electrospray ionization mass spectrometry. Anal. Chem. 83, 6738-6745
    • (2011) Anal. Chem. , vol.83 , pp. 6738-6745
    • Walker, S.H.1    Budhathoki-Uprety, J.2    Novak, B.M.3    Muddiman, D.C.4
  • 29
    • 77950421797 scopus 로고    scopus 로고
    • Comparative glycomics using a tetraplex stable-isotope coded tag
    • Bowman, M. J., and Zaia, J. (2010) Comparative glycomics using a tetraplex stable-isotope coded tag. Anal. Chem. 82, 3023-3031
    • (2010) Anal. Chem. , vol.82 , pp. 3023-3031
    • Bowman, M.J.1    Zaia, J.2
  • 30
    • 66249114347 scopus 로고    scopus 로고
    • N-Glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C
    • Gil, G. C., Velander, W. H., and Van Cott, K. E. (2009) N-Glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Proteomics 9, 2555-2567
    • (2009) Proteomics , vol.9 , pp. 2555-2567
    • Gil, G.C.1    Velander, W.H.2    Van Cott, K.E.3
  • 32
    • 79954616758 scopus 로고    scopus 로고
    • Ultrasensitive characterization of site-specific glycosylation of affinity-purified haptoglobin from lung cancer patient plasma using 10 μm i.d. porous layer open tubular liquid chromatography-linear ion trap collision-induced dissociation/electron transfer dissociation mass spectrometry
    • Wang, D., Hincapie, M., Rejtar, T., and Karger, B. L. (2011) Ultrasensitive characterization of site-specific glycosylation of affinity-purified haptoglobin from lung cancer patient plasma using 10 μm i.d. porous layer open tubular liquid chromatography-linear ion trap collision-induced dissociation/electron transfer dissociation mass spectrometry. Anal. Chem. 83, 2029-2037
    • (2011) Anal. Chem. , vol.83 , pp. 2029-2037
    • Wang, D.1    Hincapie, M.2    Rejtar, T.3    Karger, B.L.4
  • 33
    • 13444288238 scopus 로고    scopus 로고
    • Identification of Lewis x structures of the cell adhesion molecule CEACAM1 from human granulocytes
    • DOI 10.1093/glycob/cwh139
    • Lucka, L., Fernando, M., Grunow, D., Kannicht, C., Horst, A. K., Nollau, P., and Wagener, C. (2005) Identification of Lewis x structures of the cell adhesion molecule CEACAM1 from human granulocytes. Glycobiology 15, 87-100 (Pubitemid 40202042)
    • (2005) Glycobiology , vol.15 , Issue.1 , pp. 87-100
    • Lucka, L.1    Fernanado, M.2    Grunow, D.3    Kannicht, C.4    Horst, A.K.5    Nollau, P.6    Wagener, C.7
  • 35
    • 33749045903 scopus 로고    scopus 로고
    • Decoding sugar functions by identifying target glycoproteins
    • DOI 10.1016/j.sbi.2006.08.011, PII S0959440X06001461, Carbohydrates and Glycoconjugates / Biophysical Methods
    • Taniguchi, N., Miyoshi, E., Gu, J., Jianguo, G., Honke, K., and Matsumoto, A. (2006) Decoding sugar functions by identifying target glycoproteins. Curr. Opin. Struct. Biol. 16, 561-566 (Pubitemid 44466412)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.5 , pp. 561-566
    • Taniguchi, N.1    Miyoshi, E.2    Jianguo, G.3    Honke, K.4    Matsumoto, A.5
  • 36
    • 77956160217 scopus 로고    scopus 로고
    • Lectin-based glycoproteomic techniques for the enrichment and identification of potential biomarkers
    • Abbott, K. L., and Pierce, J. M. (2010) Lectin-based glycoproteomic techniques for the enrichment and identification of potential biomarkers. Methods Enzymol. 480, 461-476
    • (2010) Methods Enzymol. , vol.480 , pp. 461-476
    • Abbott, K.L.1    Pierce, J.M.2
  • 37
    • 33751383272 scopus 로고    scopus 로고
    • Site-specific glycan analysis of human chorionic gonadotropin β-subunit from malignancies and pregnancy by liquid chromatography - Electrospray mass spectrometry
    • DOI 10.1093/glycob/cwl034
    • Valmu, L., Alfthan, H., Hotakainen, K., Birken, S., and Stenman, U. H. (2006) Site-specific glycan analysis of human chorionic gonadotropin β-subunit from malignancies and pregnancy by liquid chromatography- electrospray mass spectrometry. Glycobiology 16, 1207-1218 (Pubitemid 44811584)
    • (2006) Glycobiology , vol.16 , Issue.12 , pp. 1207-1218
    • Valmu, L.1    Alfthan, H.2    Hotakainen, K.3    Birken, S.4    Stenman, U.-H.5
  • 38
    • 33749253578 scopus 로고    scopus 로고
    • Dynamic profiling of the post-translational modifications and interaction partners of epidermal growth factor receptor signaling after stimulation by epidermal growth factor using Extended Range Proteomic Analysis (ERPA)
    • DOI 10.1074/mcp.M600105-MCP200
    • Wu, S. L., Kim, J., Bandle, R. W., Liotta, L., Petricoin, E., and Karger, B. L. (2006) Dynamic profiling of the post-translational modifications and interaction partners of epidermal growth factor receptor signaling after stimulation by epidermal growth factor using extended range proteomic analysis (ERPA). Mol. Cell. Proteomics 5, 1610-1627 (Pubitemid 44480389)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.9 , pp. 1610-1627
    • Wu, S.-L.1    Kim, J.2    Bandle, R.W.3    Liotta, L.4    Petricoin, E.5    Karger, B.L.6
  • 39
    • 84863794084 scopus 로고    scopus 로고
    • Glycomic and proteomic profiling of pancreatic cyst fluids identifies hyperfucosylated lactosamines on the N-linked glycans of overexpressed glycoproteins
    • Mann, B. F., Goetz, J. A., House, M. G., Schmidt, C. M., and Novotny, M. V. (2012) Glycomic and proteomic profiling of pancreatic cyst fluids identifies hyperfucosylated lactosamines on the N-linked glycans of overexpressed glycoproteins. Mol. Cell. Proteomics 11, M111.015792
    • (2012) Mol. Cell. Proteomics , vol.11
    • Mann, B.F.1    Goetz, J.A.2    House, M.G.3    Schmidt, C.M.4    Novotny, M.V.5
  • 40
    • 50449103968 scopus 로고    scopus 로고
    • Fucosylated haptoglobin is a novel marker for pancreatic cancer: Detailed analyses of oligosaccharide structures
    • Miyoshi, E., and Nakano, M. (2008) Fucosylated haptoglobin is a novel marker for pancreatic cancer: Detailed analyses of oligosaccharide structures. Proteomics 8, 3257-3262
    • (2008) Proteomics , vol.8 , pp. 3257-3262
    • Miyoshi, E.1    Nakano, M.2
  • 42
    • 84857881654 scopus 로고    scopus 로고
    • a1-3/4 fucosylation at Asn 241 of ss-haptoglobin is a novel marker for colon cancer: A combinatorial approach for development of glycan biomarkers
    • Park, S. Y., Lee, S. H., Kawasaki, N., Itoh, S., Kang, K., Hee Ryu, S., Hashii, N., Kim, J. M., Kim, J. Y., and Hoe Kim, J. (2012) a1-3/4 fucosylation at Asn 241 of ss-haptoglobin is a novel marker for colon cancer: A combinatorial approach for development of glycan biomarkers. Int. J. Cancer 130, 2366-2376
    • (2012) Int. J. Cancer , vol.130 , pp. 2366-2376
    • Park, S.Y.1    Lee, S.H.2    Kawasaki, N.3    Itoh, S.4    Kang, K.5    Hee Ryu, S.6    Hashii, N.7    Kim, J.M.8    Kim, J.Y.9    Hoe Kim, J.10
  • 43
    • 46349088505 scopus 로고    scopus 로고
    • Biological function of fucosylation in cancer biology
    • DOI 10.1093/jb/mvn011
    • Miyoshi, E., Moriwaki, K., and Nakagawa, T. (2008) Biological function of fucosylation in cancer biology. J. Biochem. 143, 725-729 (Pubitemid 351918934)
    • (2008) Journal of Biochemistry , vol.143 , Issue.6 , pp. 725-729
    • Miyoshi, E.1    Moriwaki, K.2    Nakagawa, T.3
  • 46
    • 81255144234 scopus 로고    scopus 로고
    • Fragmentation and site-specific quantification of core fucosylated glycoprotein by multiple reaction monitoring-mass spectrometry
    • Zhao, Y., Jia, W., Wang, J., Ying, W., Zhang, Y., and Qian, X. (2011) Fragmentation and site-specific quantification of core fucosylated glycoprotein by multiple reaction monitoring-mass spectrometry. Anal. Chem. 83, 8802-8809
    • (2011) Anal. Chem. , vol.83 , pp. 8802-8809
    • Zhao, Y.1    Jia, W.2    Wang, J.3    Ying, W.4    Zhang, Y.5    Qian, X.6
  • 47
    • 34748916981 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: A critical review
    • DOI 10.1007/s00216-007-1486-6, Proteomics/Molecular Imaging
    • Bantscheff, M., Schirle, M., Sweetman, G., Rick, J., and Kuster, B. (2007) Quantitative mass spectrometry in proteomics: a critical review. Anal. Bioanal. Chem. 389, 1017-1031 (Pubitemid 47482251)
    • (2007) Analytical and Bioanalytical Chemistry , vol.389 , Issue.4 , pp. 1017-1031
    • Bantscheff, M.1    Schirle, M.2    Sweetman, G.3    Rick, J.4    Kuster, B.5
  • 48
    • 44449153943 scopus 로고    scopus 로고
    • Functional roles of N-glycans in cell signaling and cell adhesion in cancer
    • DOI 10.1111/j.1349-7006.2008.00839.x
    • Zhao, Y. Y., Takahashi, M., Gu, J. G., Miyoshi, E., Matsumoto, A., Kitazume, S., and Taniguchi, N. (2008) Functional roles of N-glycans in cell signaling and cell adhesion in cancer. Cancer Sci. 99, 1304-1310 (Pubitemid 351761717)
    • (2008) Cancer Science , vol.99 , Issue.7 , pp. 1304-1310
    • Zhao, Y.-Y.1    Takahashi, M.2    Gu, J.-G.3    Miyoshi, E.4    Matsumoto, A.5    Kitazume, S.6    Taniguchi, N.7


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